5W7B

Rabbit acyloxyacyl hydrolase (AOAH), proteolytically processed, S262A mutant, with LPS

5W7B の概要

• エントリーDOI: 10.2210/pdb5w7b/pdb
• 分子名称: Acyloxyacyl hydrolase small subunit, MYRISTIC ACID, CALCIUM ION, ... (16 entities in total)
• 機能のキーワード: lipopolysaccharide, lps, gdsl esterase, saposin, hydrolase
• 由来する生物種: Oryctolagus cuniculus (Rabbit); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 139339.23

構造登録者

Gorelik, A.,Illes, K.,Nagar, B. (登録日: 2017-06-19, 公開日: 2018-01-03, 最終更新日: 2024-11-13)

主引用文献

Gorelik, A.,Illes, K.,Nagar, B.
Crystal structure of the mammalian lipopolysaccharide detoxifier.
Proc. Natl. Acad. Sci. U.S.A., 115:E896-E905, 2018

PubMed Abstract: LPS is a potent bacterial endotoxin that triggers the innate immune system. Proper recognition of LPS by pattern-recognition receptors requires a full complement of typically six acyl chains in the lipid portion. Acyloxyacyl hydrolase (AOAH) is a host enzyme that removes secondary (acyloxyacyl-linked) fatty acids from LPS, rendering it immunologically inert. This activity is critical for recovery from immune tolerance that follows Gram-negative infection. To understand the molecular mechanism of AOAH function, we determined its crystal structure and its complex with LPS. The substrate's lipid moiety is accommodated in a large hydrophobic pocket formed by the saposin and catalytic domains with a secondary acyl chain inserted into a narrow lateral hydrophobic tunnel at the active site. The enzyme establishes dispensable contacts with the phosphate groups of LPS but does not interact with its oligosaccharide portion. Proteolytic processing allows movement of an amphipathic helix possibly involved in substrate access at membranes.

PubMed: 29343645
DOI: 10.1073/pnas.1719834115

実験手法

X-RAY DIFFRACTION (1.9 Å)